Protein kinase structural properties

Takahashi 1, Saitoh Y, Yoshida M, Sano H, Nakano H, Morimoto M, Tamaoki T. (1989) UCN-01 and UCN-02, new selective inhibitors of protein kinase C. 11. Purification, physico-chemical properties, structural determination and biological activities. J Antibiot 42 571-576. 

Similar application to the construction of bisindole system was reported by Faul and co-workers. That is, the core structure (indole[2,3-a]carbazoles) (165) of rebeccamycin (61), which possesses potent antitumor and protein kinase C inhibitory properties, was synthesized by intramolecular coupling reaction of bisindolylmaleimides (164) with PIFA-BF3 Et20 [127] (Scheme 34). 

The role of calcium in regulating cardiovascular physiology is presented in the fourth section of this volume. House et al. have provided an excellent review on the structure of calmodulin-dependent protein kinase II and its role in the contractility as well as proliferation and migration of VSMC. Banderali et al. have examined in detail the cellular regulation and pharmacological properties of calcium-activated potassium channels and their role in control of vascular tone by endothelium. 

A biologic reason for the abundance of nonlamellar lipids in membranes is that they possess the ability to modulate the activities of membrane proteins (15, 16). It has been recognized that membranes exist in a state of curvature frustration, which may be sufficiently large to have significant effect on certain protein conformations (17). Many examples show that the lipid bilayer elastic curvature stress indeed couples to conformational changes of membrane proteins (15, 18, 19). Protein kinase C is one such example of an enzyme activated by lipids that exhibit a propensity for nonlamellar phase formation (20). The activity of Ca " -ATPase from sarcoplasmic reticulum membranes also strongly correlates with the occurrence of nonbilayer lipids in the membrane and increases with the increase of their amount. It is noteworthy that the protein activity does not depend on the chemical structure of the lipids but only on their phase propensity thus specific binding interactions are ruled out. The list of proteins with activities that depend on the phase properties... 

Reversible covalent modification. The catalytic properties of many enzymes are markedly altered by the covalent attachment of a modifying group, most commonly a phosphoryl group. ATP serves as the phosphoryl donor in these reactions, which are catalyzed by protein kinases. The removal of phosphoryl groups by hydrolysis is catalyzed by protein phosphatases. This chapter considers the structure, specificity, and control of protein kinase A (PKA), a ubiquitous eukaryotic enzyme that regulates diverse target proteins. 

Isozymes are enzyme variants that catalyze the same reaction but are structurally different (they are coded by separate gene loci). Allozymes are variants that arise due to polymorphism at a single gene locus. Isozymes can vary enormously in their properties (e.g., substrate affinities, responses to allosteric effectors, phosphorylation by protein kinases) to support the different functional needs for a particular reaction in different organs or different compartments of the cell (e.g., mitochon-... 

The Ser/Thr- and Tyr-specific protein kinases share many common features. The catalytic mechanism, structural properties and mechanisms of kinase control are very similar for the two kinase classes. In the following, the main properties of both classes will therefore be presented together (reviews Johnson et al., 1998 Engh and Bosse-meyer, 2001). ... 

Ono Y, Fuji T, Ogita K, Kikkawa U, Igarashi K, Nishizuka Y (1988) The structure, expression, and properties of additional members of the protein kinase C family. J. Biol. Chem., 263, 6927 932. 

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